Please use this identifier to cite or link to this item: https://doi.org/10.1021/bm034101b
Title: Eggshell matrix protein mimics: Designer peptides to induce the nucleation of calcite crystal aggregates in solution
Authors: Ajikumar, P.K. 
Lakshminarayanan, R. 
Ong, B.T.
Valiyaveettil, S. 
Manjunatha Kini, R. 
Issue Date: Sep-2003
Source: Ajikumar, P.K., Lakshminarayanan, R., Ong, B.T., Valiyaveettil, S., Manjunatha Kini, R. (2003-09). Eggshell matrix protein mimics: Designer peptides to induce the nucleation of calcite crystal aggregates in solution. Biomacromolecules 4 (5) : 1321-1326. ScholarBank@NUS Repository. https://doi.org/10.1021/bm034101b
Abstract: Ansocalcin is a novel goose eggshell matrix protein with 132 amino acid residues, which induces the formation of polycrystalline calcite aggregates in in vitro crystallization experiments. The central region of ansocalcin is characterized by the presence of multiplets of charged amino acids. To investigate the specific role of charged amino acid multiplets in the crystal nucleation, three short peptides REWD-16, REWDP-17 (containing charged doublets), and RADA-16 (alternating charged residues) were synthesized and characterized. The aggregation of these peptides in solution was investigated using circular dichroism, intrinsic tryptophan fluorescence, and dynamic light scattering experiments. The peptides REWD-16 and REWDP-17 induced the polycrystalline calcite crystal aggregates, whereas RADA-16 did not induce significant changes in calcite crystal morphology or aggregate formation in in vitro crystallization experiments. The lattice and morphology of the calcite crystals were characterized using X-ray diffraction and scanning electron microscope. The results discussed in this paper reveal the importance of multiplets of charged amino acid residues toward the nucleation of polycrystalline calcite crystal aggregates in solution.
Source Title: Biomacromolecules
URI: http://scholarbank.nus.edu.sg/handle/10635/52899
ISSN: 15257797
DOI: 10.1021/bm034101b
Appears in Collections:Staff Publications

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